HDAC1 Antibody (YA395),MedChemexpress,HY-P80149

HDAC1 is a histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of core histones (H2A, H2B, H3, and H4). Histone deacetylation serves as an epigenetic repression tag and plays a critical role in transcriptional regulation, cell cycle progression, and developmental events. HDAC1 functions by forming large multiprotein complexes and is a component of the NuRD histone deacetylase complex, which participates in chromatin remodeling. As part of the SIN3B complex, it is recruited downstream of constitutively active gene transcription start sites through histone interactions, mitigating histone acetylation and RNA polymerase II progression within transcribed regions to regulate transcription. HDAC1 also acts as a deacetylase for non-histone targets, including NR1D2, RELA, SP1, SP3, STAT3, and TSHZ3. It deacetylates SP proteins (SP1 and SP3) to regulate their function. Additionally, HDAC1 is a component of the BRG1-RB1-HDAC1 complex, which negatively regulates CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex, allowing CREBBP recruitment to facilitate transcriptional activation. HDAC1 deacetylates TSHZ3 to modulate its transcriptional repressor activity, deacetylates 'Lys-310' in RELA to inhibit NF-kappa-B transcriptional activity, and deacetylates NR1D2 to counteract KAT5-mediated relief of NR1D2 transcriptional repression. By similarity, HDAC1 is part of an RCOR/GFI/KDM1A/HDAC complex that suppresses genes involved in multilineage blood cell development via histone deacetylase recruitment. It is also involved in CIART-mediated repression of the CLOCK-BMAL1 heterodimer and required for transcriptional repression of circadian target genes (e.g., PER1) by large PER or CRY1 complexes through histone deacetylation. Beyond protein deacetylase activity, HDAC1 exhibits protein-lysine deacylase activity, functioning as a decrotonylase and delactylase to mediate histone decrotonylation ((2E)-butenoyl) and delactylation (lactoyl), respectively.